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Database: UniProt
Entry: C4ZPW3
LinkDB: C4ZPW3
Original site: C4ZPW3 
ID   CAIC_ECOBW              Reviewed;         517 AA.
AC   C4ZPW3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   26-NOV-2014, entry version 42.
DE   RecName: Full=Probable crotonobetaine/carnitine-CoA ligase {ECO:0000255|HAMAP-Rule:MF_01524};
DE            EC=6.2.1.- {ECO:0000255|HAMAP-Rule:MF_01524};
GN   Name=caiC {ECO:0000255|HAMAP-Rule:MF_01524};
GN   OrderedLocusNames=BWG_0035;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/JB.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L.,
RA   Reeves P.R., Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational
RT   events in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(2009).
CC   -!- FUNCTION: Could catalyze the transfer of CoA to carnitine,
CC       generating the initial carnitinyl-CoA needed for the CaiB reaction
CC       cycle. {ECO:0000255|HAMAP-Rule:MF_01524}.
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_01524}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. {ECO:0000255|HAMAP-Rule:MF_01524}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACR64209.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP001396; ACR64209.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_002925238.1; NC_012759.1.
DR   ProteinModelPortal; C4ZPW3; -.
DR   SMR; C4ZPW3; 20-517.
DR   STRING; 595496.BWG_0035; -.
DR   EnsemblBacteria; ACR64209; ACR64209; BWG_0035.
DR   GeneID; 7953163; -.
DR   KEGG; ebw:BWG_0035; -.
DR   PATRIC; 18268946; VBIEscCol60876_0037.
DR   eggNOG; COG0318; -.
DR   HOGENOM; HOG000230001; -.
DR   KO; K02182; -.
DR   OMA; ESEWILQ; -.
DR   OrthoDB; EOG6MH5BV; -.
DR   BioCyc; ECOL595496:GI18-37-MONOMER; -.
DR   UniPathway; UPA00117; -.
DR   GO; GO:0016878; F:acid-thiol ligase activity; IEA:InterPro.
DR   GO; GO:0051108; F:carnitine-CoA ligase activity; IEA:InterPro.
DR   GO; GO:0051109; F:crotonobetaine-CoA ligase activity; IEA:InterPro.
DR   GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01524; CaiC; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR023456; CaiC.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Ligase.
FT   CHAIN         1    517       Probable crotonobetaine/carnitine-CoA
FT                                ligase.
FT                                /FTId=PRO_0000383395.
SQ   SEQUENCE   517 AA;  58559 MW;  C7A307D16200D8E9 CRC64;
     MDIIGGQHLR QMWDDLADVY GHKTALICES SGGVVNRYSY LELNQEINRT ANLFYTLGIR
     KGDKVALHLD NCPEFIFCWF GLAKIGAIMV PINARLLCEE SAWILQNSQA CLLVTSAQFY
     PMYQQIQQED ATQLRHICLT DVALPADDGV SSFTQLKNQQ PATLCYAPPL STDDTAEILF
     TSGTTSRPKG VVITHYNLRF AGYYSAWQCA LRDDDVYLTV MPAFHIDCQC TAAMAAFSAG
     ATFVLVEKYS ARAFWGQVQK YRATVTECIP MMIRTLMVQP PSANDQQHRL REVMFYLNLS
     EQEKDAFCER FGVRLLTSYG MTETIVGIIG DRPGDKRRWP SIGRVGFCYE AEIRDDHNRP
     LPAGEIGEIC IKGIPGKTIF KEYFLNPQAT AKVLEADGWL HTGDTGYRDE EDFFYFVDRR
     CNMIKRGGEN VSCVELENII AAHPKIQDIV VVGIKDSIRD EAIKAFVVLN EGETLSEEEF
     FRFCEQNMAK FKVPSYLEIR KDLPRNCSGK IIRKNLK
//
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